[Aerobic metabolism of VX and mixed function oxidases].
In our preliminary study, it has been found that VX oxidase exists in the microsome fraction of rat liver and the catalytic reaction needs the participation of molecular oxygen and coenzyme I or II. In this paper, the data showed that deoxycholate inactivated both the mixed function oxidase and VX oxidase. The specific inhibitor proadifen of the mixed function oxidase also profoundly inhibited VX oxidase activity. The complex of VX and cytochrome P-450 exhibited typical difference spectrum of type I. Aniline competitively inhibited the inactivation of VX catalyzed by microsomes. These results indicate that VX is one of the substrates of mixed function oxidase. VX oxidase in the rat liver cells is exactly the mixed function oxidase.
Fu
F H
FH
Institute of Pharmacology and Toxicology, Academy of Military Medical Sciences, Beijing, China.
Sun
M J
MJ
D000332:Aerobiosis; D000818:Animals; D002800:Cholinesterase Inhibitors / Q000378:metabolism*; D003840:Deoxycholic Acid / Q000494:pharmacology; D008099:Liver / Q000201:enzymology; D008297:Male; D008862:Microsomes, Liver / Q000201:enzymology; D006899:Mixed Function Oxygenases / Q000378:metabolism*; D009946:Organothiophosphorus Compounds / Q000378:metabolism*; D011335:Proadifen / Q000494:pharmacology*; D051381:Rats; D011919:Rats, Inbred Strains
D002800:Cholinesterase Inhibitors; D003840:Deoxycholic Acid; D006899:Mixed Function Oxygenases; D009946:Organothiophosphorus Compounds; D011335:Proadifen; C009680:VX-agent